Protein structure modification and allergenic properties of whey proteins upon interaction with tea and coffee phenolic compounds

Journal of Functional Foods

Ana Carolina M. Figueira¹  Tássia B. Pessato²  Flavia M. Netto²  Natália C. de Carvalho²  Francielli P.R. de Morais²  Ricardo de L. Zollner³  Luís Gustavo R. Fernandes³ 

[1] Brazilian Biosciences National Laboratory, Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, São Paulo, Brazil;Department of Food and Nutrition, School of Food Engineering, University of Campinas, São Paulo, Brazil;Laboratory of Translational Immunology, School of Medical Sciences, University of Campinas, São Paulo, Brazil;

关键词: Protein-phenolic interactions;    Soluble complexes;    Cow’s milk allergy;    Hypoallergenic products;    ELISA;   

DOI  :  

来源: DOAJ

【 摘 要 】

Structural changes and allergenicity of whey proteins (WPI) upon complexation with caffeic acid (CA) and (-)-epigallocatechin gallate (EGCG) at acidic and neutral pH conditions were investigated. WPI-phenolic compounds interactions were evidenced by fluorescence quenching, accompanied by red-shift (32 nm in WPI-CA and 3 nm in WPI-EGCG). Negative exothermic enthalpy obtained by isothermal titration calorimetry analysis (–5966.4 ± 733.7 kJ/mol for WPI-CA and −14378.3 ± 2363.8 kJ/mol for WPI-EGCG) and reduction of surface hydrophobicity suggest that those interactions are of non-covalent nature. Additionally, changes in secondary structure pattern and increase in thermal stability were demonstrated by circular dichroism and were higher in neutral than in acidic conditions. WPI-EGCG complexes obtained in both pH conditions showed a reduced IgE-binding capacity to β-lg and BSA, two important allergens in milk. In conclusion, we suggest that complexation with EGCG could be a promising strategy to reduce the allergenicity of whey proteins.

【 授权许可】

Unknown